Carbohydrates and Sugars Quiz

A carbohydrate composed of 2 to 10 monosaccharide units linked by glycosidic bonds.

A carbohydrate composed of two monosaccharide units linked by a glycosidic bond.

A carbohydrate composed of more than 10 monosaccharide units linked by glycosidic bonds.

The simplest form of carbohydrate, consisting of a single polyhydroxy aldehyde or ketone unit.

A monosaccharide with six carbon atoms.

A hexose sugar containing a ketone group. Example: Fructose.

A hexose sugar containing an aldehyde group. Example: Glucose.

Two sugars that are mirror images of each other. They have the same chemical formula but different spatial arrangements of atoms around a chiral center.

Two sugars that differ in configuration around only one carbon atom.

Gluconic acid produced by oxidation of the aldehyde group of Glucose.

Mannitol is a sugar alcohol that is obtained by the reduction of the aldehyde group in the sugar mannose.

Glucosamine is an amino sugar derived from glucose by the addition of an amino group.

A disaccharide composed of two glucose molecules linked by an α(1→4) glycosidic bond.

A disaccharide composed of glucose and galactose linked by a β(1→4) glycosidic bond.

A disaccharide composed of glucose and fructose linked by an α(1→2) glycosidic bond.

Sucrose is a non-reducing sugar because both its anomeric carbons are involved in the glycosidic linkage.

A condition caused by the deficiency of the enzyme lactase, leading to the inability to digest lactose.

A polysaccharide composed of a single type of monosaccharide. Example: Starch, glycogen, cellulose.

The two chains of starch: Amylose and Amylopectin.

Amylopectin differs from the amylose chain by being branched, containing both α(1→4) glycosidic bonds like amylose and α(1→6) glycosidic bonds at branch points.

The storage form of carbohydrate in animals. Structurally similar to amylopectin but more highly branched.

Cellulose cannot be hydrolysed in humans because it contains β(1→4) glycosidic bonds, while human digestive enzymes can only break down α glycosidic bonds.

Cellulose is a linear polymer of glucose units linked by β(1→4) glycosidic bonds.

A large molecule formed by the binding of glycosaminoglycans to a protein core.

Hyaluronic acid is a glycosaminoglycan that is sulphate-free.

Glycosaminoglycans are polysaccharides that attract water due to their negatively charged groups, increasing their volume and making them effective shock absorbers.

Heparin is a glycosaminoglycan that acts as an anticoagulant by preventing the formation of blood clots.

Proteoglycans contain more carbohydrate than protein, while glycoproteins contain more protein than carbohydrate.

A group of genetic disorders caused by a deficiency of lysosomal enzymes required for the degradation of glycosaminoglycans. This leads to an excessive accumulation of these substances in various tissues, causing a wide range of symptoms.

A carbon atom that is attached to four different groups of atoms.

Glycine is the smallest and simplest amino acid, lacking an asymmetric carbon atom.

Proline is an imino acid, containing a cyclic structure with a nitrogen atom.

The D and L forms of amino acids are stereoisomers. The carboxyl group attached to the alpha carbon in the D form is on the right, while in the L form it is on the left.

Amino acids that cannot be synthesized by the body and must be obtained from the diet.

Alanine is a non-essential amino acid, meaning the body can synthesize it.

Non-essential amino acids can be synthesized in the body, but not in sufficient quantities to meet the body's needs.

Compounds formed by the linkage of two or more amino acids through peptide bonds.

A tetrapeptide contains 3 peptide bonds.

A tetrapeptide contains 4 amino acids.

The peptide bond is more resistant to denaturation compared to other bonds like electrostatic bonds.

Peptide bonds can be hydrolysed by peptidase enzymes.

Glutathione is a tripeptide composed of glutamic acid, cysteine, and glycine.

Glutathione functions as an antioxidant and is involved in detoxification reactions.

Disulfide bonds are covalent bonds that form between two cysteine residues in proteins.

The primary structure of a protein is determined by the sequence of amino acids in a polypeptide chain.

The tertiary structure of a protein refers to the three-dimensional shape of the protein molecule.

Denaturation is the process of altering the native structure of a protein, leading to loss of its biological activity.

Antibodies are considered defense proteins as they recognize and bind to foreign antigens, triggering the immune response.

Glycine is an amino acid that can dissolve in water due to its polar side chain.

Histidine is a semi-essential amino acid, meaning that it is typically synthesized by the body, but in some situations, it may need to be obtained through the diet.